Copper in PDB 3nxz: Crystal Structure of Uree From Helicobacter Pylori (CU2+ Bound Form)

The structure of Crystal Structure of Uree From Helicobacter Pylori (CU2+ Bound Form), PDB code: 3nxz was solved by R.Shi, C.Munger, A.Assinas, A.Matte, M.Cygler, Montreal-Kingston Bacterialstructural Genomics Initiative (Bsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.17 / 2.70
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	88.829, 88.829, 203.635, 90.00, 90.00, 90.00
R / Rfree (%)	25.6 / 29.4

The binding sites of Copper atom in the Crystal Structure of Uree From Helicobacter Pylori (CU2+ Bound Form) (pdb code 3nxz). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Crystal Structure of Uree From Helicobacter Pylori (CU2+ Bound Form), PDB code: 3nxz:

Copper binding site 1 out of 1 in the Crystal Structure of Uree From Helicobacter Pylori (CU2+ Bound Form)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Uree From Helicobacter Pylori (CU2+ Bound Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu200 b:68.9 occ:1.00 NE2 D:HIS102 2.1 73.7 1.0 NE2 B:HIS102 2.1 77.7 1.0 NE2 A:HIS102 2.2 77.7 1.0 O C:HOH171 2.2 25.4 1.0 NE2 C:HIS102 2.5 77.1 1.0 CD2 A:HIS102 3.0 76.1 1.0 CE1 D:HIS102 3.0 71.2 1.0 CD2 B:HIS102 3.0 77.5 1.0 CE1 B:HIS102 3.1 76.8 1.0 CD2 D:HIS102 3.1 73.6 1.0 CD2 C:HIS102 3.3 77.6 1.0 CE1 A:HIS102 3.3 74.9 1.0 CE1 C:HIS102 3.6 78.3 1.0 ND1 D:HIS102 4.1 70.3 1.0 ND1 B:HIS102 4.1 75.3 1.0 CG B:HIS102 4.2 74.5 1.0 CG D:HIS102 4.2 71.1 1.0 CG A:HIS102 4.2 71.8 1.0 ND1 A:HIS102 4.3 72.2 1.0 CG C:HIS102 4.5 75.1 1.0 ND1 C:HIS102 4.7 78.7 1.0 O A:ASN100 4.8 73.6 1.0

R.Shi, C.Munger, A.Asinas, S.L.Benoit, E.Miller, A.Matte, R.J.Maier, M.Cygler. Crystal Structures of Apo and Metal-Bound Forms of the Uree Protein From Helicobacter Pylori: Role of Multiple Metal Binding Sites Biochemistry V. 49 7080 2010.
ISSN: ISSN 0006-2960
PubMed: 20681615
DOI: 10.1021/BI100372H